Human respiratory syncytial (RS) virus encodes two envelope-associated glycoproteins, the fusion (F) glycoprotein and the larger (G) glycoprotein. As described previously, the complete amino sequence of the F glycoprotein was deduced by nucleotide sequence analysis of a nearly-complete cDNA of the mRNA. Recently, a complete cDNA of the mRNA encoding the G glycoprotein was isolated and analyzed by DNA sequencing. The predicted mRNA sequence encodes a protein of 298 amino acids, consistent with the estimated molecular weight of the in vitro translation product synthesized in response to hybrid-selected mRNA. Taken together with results from other laboratories, the predicted amino acid sequence shows that the G glycoprotein contains a remarkably high content of N-linked and O-linked carbohydrate and probably is anchored in the membrane by a hydrophobic domain located near the N-terminus.